Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Vetting, M.W.; Wackett, L.P.; Que, L.Jr.; Lipscomb, J.D.; Ohlendorf, D.H.
    Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases (2004), J. Bacteriol., 186, 1945-1958.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.15 Fe2+ located in C-terminal barrel Brevibacterium fuscum
1.13.11.15 Mn2+
-
 Arthrobacter globiformis

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.15 Arthrobacter globiformis
-
-
-
1.13.11.15 Brevibacterium fuscum
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.15 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde mechanism, substrate chelates the metal ion asymmetrically at sites trans to two imidazole ligands Arthrobacter globiformis
a
1.13.11.15 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde mechanism, substrate chelates the metal ion asymmetrically at sites trans to two imidazole ligands Brevibacterium fuscum
a

Subunits

EC Number Subunits Comment Organism
1.13.11.15 homotetramer crystallization data Arthrobacter globiformis
1.13.11.15 homotetramer crystallization data Brevibacterium fuscum